title: Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.
abstract: Alpha-synuclein is analyzed in physiological conditions by CLEANEX-PM methodology, in which the amide-proton exchange can be monitored at millisecond scale. The relationship between kex and [OH](-) is confirmed as a linear correlation with slope 1, indicating EX2 regime. There are significant residual structures at the N- and C-terminal regions. The structure at the C-terminal region is more stable than that of the N-terminal region. The middle part including NAC region is not completely protected. The data acquired at various pH and mixing time conditions followed by linear fitting give accurate information about residual structures.
authors.affiliation: Faculty of Pharmaceutical Sciences, Teikyo Heisei University, Nakano, Tokyo 164-8530, Japan.
authors.forename: Honoka
authors.initials: H
authors.lastname: Okazaki
authors.forename: Yuka
authors.initials: Y
authors.lastname: Ohori
authors.forename: Masaya
authors.initials: M
authors.lastname: Komoto
authors.forename: Young-Ho
authors.initials: YH
authors.lastname: Lee
authors.forename: Yuji
authors.initials: Y
authors.lastname: Goto
authors.forename: Naoya
authors.initials: N
authors.lastname: Tochio
authors.forename: Chiaki
authors.initials: C
authors.lastname: Nishimura
mesh_terms: D006801:Humans; D006863:Hydrogen-Ion Concentration; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017510:Protein Folding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D051844:alpha-Synuclein
keywords: Alpha-synuclein; Amide proton exchange; NMR; Protein folding; Unfolded protein